ACSF4_DROME
ID ACSF4_DROME Reviewed; 1012 AA.
AC Q9VLL0; Q1RKX6; Q9U973;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 3.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Beta-alanine-activating enzyme {ECO:0000250|UniProtKB:Q80WC9};
DE EC=6.2.1.- {ECO:0000250|UniProtKB:Q80WC9};
DE AltName: Full=Acyl-CoA synthetase family member 4;
GN Name=Aasdh {ECO:0000312|FlyBase:FBgn0027780};
GN Synonyms=U26 {ECO:0000312|FlyBase:FBgn0027780};
GN ORFNames=CG13401 {ECO:0000312|FlyBase:FBgn0027780};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Antenna;
RA Hovemann B.T., Heiermann R., Malz J., Richardt A., Stoertkuhl K.F.,
RA Sehlmeyer F.;
RT "Deliniation of a modular structered enhancer that gives rise to olfactory
RT organ specific expression of Drosophila1-acylglycerol-3-phosphate O-
RT acyltransferase.";
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Covalently binds beta-alanine in an ATP-dependent manner to
CC form a thioester bond with its phosphopantetheine group and transfers
CC it to an, as yet, unknown acceptor. May be required for a post-
CC translational protein modification or for post-transcriptional
CC modification of an RNA. {ECO:0000250|UniProtKB:Q80WC9}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABE73255.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB53510.1; Type=Miscellaneous discrepancy; Note=Insertion of a few bases causing frameshift at residue 295.; Evidence={ECO:0000305};
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DR EMBL; AJ245708; CAB53510.1; ALT_SEQ; mRNA.
DR EMBL; AE014134; AAF52679.3; -; Genomic_DNA.
DR EMBL; BT025084; ABE73255.1; ALT_SEQ; mRNA.
DR RefSeq; NP_609230.2; NM_135386.5.
DR RefSeq; NP_995660.2; NM_205938.2.
DR AlphaFoldDB; Q9VLL0; -.
DR SMR; Q9VLL0; -.
DR STRING; 7227.FBpp0088615; -.
DR PaxDb; Q9VLL0; -.
DR PRIDE; Q9VLL0; -.
DR DNASU; 34175; -.
DR EnsemblMetazoa; FBtr0089673; FBpp0088615; FBgn0027780.
DR EnsemblMetazoa; FBtr0340243; FBpp0309217; FBgn0027780.
DR GeneID; 34175; -.
DR KEGG; dme:Dmel_CG13401; -.
DR UCSC; CG13401-RA; d. melanogaster.
DR CTD; 132949; -.
DR FlyBase; FBgn0027780; Aasdh.
DR VEuPathDB; VectorBase:FBgn0027780; -.
DR eggNOG; KOG1178; Eukaryota.
DR eggNOG; KOG4649; Eukaryota.
DR GeneTree; ENSGT00440000033811; -.
DR HOGENOM; CLU_010423_0_0_1; -.
DR InParanoid; Q9VLL0; -.
DR OMA; GEKPIFA; -.
DR PhylomeDB; Q9VLL0; -.
DR BioGRID-ORCS; 34175; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 34175; -.
DR PRO; PR:Q9VLL0; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0027780; Expressed in egg cell and 20 other tissues.
DR ExpressionAtlas; Q9VLL0; baseline and differential.
DR Genevisible; Q9VLL0; DM.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003833; F:beta-alanyl amine synthase activity; ISS:FlyBase.
DR GO; GO:0043041; P:amino acid activation for nonribosomal peptide biosynthetic process; IBA:GO_Central.
DR GO; GO:0006631; P:fatty acid metabolic process; ISS:UniProtKB.
DR Gene3D; 2.130.10.10; -; 2.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR018391; PQQ_beta_propeller_repeat.
DR InterPro; IPR002372; PQQ_repeat.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13360; PQQ_2; 1.
DR SMART; SM00564; PQQ; 5.
DR SUPFAM; SSF50998; SSF50998; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Fatty acid metabolism; Ligase; Lipid metabolism;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..1012
FT /note="Beta-alanine-activating enzyme"
FT /id="PRO_0000315806"
FT BINDING 177..185
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 411
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 426
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 516
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT CONFLICT 63
FT /note="K -> M (in Ref. 4; ABE73255)"
FT /evidence="ECO:0000305"
FT CONFLICT 123
FT /note="A -> V (in Ref. 4; ABE73255)"
FT /evidence="ECO:0000305"
FT CONFLICT 169
FT /note="A -> G (in Ref. 4; ABE73255)"
FT /evidence="ECO:0000305"
FT CONFLICT 199
FT /note="V -> M (in Ref. 4; ABE73255)"
FT /evidence="ECO:0000305"
FT CONFLICT 267
FT /note="T -> S (in Ref. 4; ABE73255)"
FT /evidence="ECO:0000305"
FT CONFLICT 286
FT /note="D -> E (in Ref. 4; ABE73255)"
FT /evidence="ECO:0000305"
FT CONFLICT 309
FT /note="V -> D (in Ref. 4; ABE73255)"
FT /evidence="ECO:0000305"
FT CONFLICT 417
FT /note="Q -> H (in Ref. 4; ABE73255)"
FT /evidence="ECO:0000305"
FT CONFLICT 424
FT /note="S -> N (in Ref. 4; ABE73255)"
FT /evidence="ECO:0000305"
FT CONFLICT 638
FT /note="T -> P (in Ref. 4; ABE73255)"
FT /evidence="ECO:0000305"
FT CONFLICT 642
FT /note="V -> A (in Ref. 4; ABE73255)"
FT /evidence="ECO:0000305"
FT CONFLICT 744
FT /note="N -> D (in Ref. 4; ABE73255)"
FT /evidence="ECO:0000305"
FT CONFLICT 912
FT /note="L -> V (in Ref. 4; ABE73255)"
FT /evidence="ECO:0000305"
FT CONFLICT 970
FT /note="F -> L (in Ref. 4; ABE73255)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1012 AA; 113084 MW; 765A7CA3EFF9B703 CRC64;
MIPSDMDLIE STAEQPDKLY NINRIRAFKD VPFLIRRTES KDTIVSYADA ADEIQVLMNF
LRKNGVPDEA GIALRVTEHT PASSLMILAI LNNKCHFFPT DKMMLSQDLY SQMSTAGVDY
LVANKHLTVA PLYFTFLGSI LVFKEDCRLY RVKLKSADET VQSKKPLPAN MCYTISTTGT
TGKPKLIHVP YECIAPNIVG LSQKLNVSMA DIIYLGTPIT FDPFVVEFFL ALQNGATLLT
SRHSMRDSPS KVLSALFPDN LATPGITVLQ MTPSLFRQFG ASSIKDRVLS GSSSLRVLLL
GGEPFPSNVE LVTWMHPSVL MQKHICNIYG ITEISCWSLL HIVQSLQSPV PLGTPIEEDT
VLRIESEDNE TSQQGELFLG SVKRRCYIPE VDDQANASQD DSGICFRATG DLVTRQQDGT
LFYSERSNDV VKRAGNRISL GLITRKIQKC LPSSELTTCL WLEDLQKLIC CIRTLESKTR
VQQRVQTFDI LSKVSIAEQP DRFVYLQHFP CNVHGKLDKQ QLLKMCIPLA QPAQQILKSY
LHDRLECVEE PDDSASKKQR LDDAAPCGYD LSFRQAGGTS FHAITICREI GLQMCIDDEQ
RHLFEMLLDE NIPLRTVLRF LDTAKLVANN IKRKNVETAV VVSACQSGLI IKRIEQPVLK
LQIYWKVNFE KCIDSPVTEY EGRFICVGAH SKILRTLNPQ TGSEYSVVKL PERIECKVTF
LTEQLAMVGC YDGCLYGFNP QTGNIVFRVG IGGLIKSQPM LTADGRRIIV CSYADDYNVY
CLSAERQEVL WCLRIGEKPI FASPLELPRE QSLIVCTLDG SYSRVAITDG SVEWTQKFRE
PVFSTPVLLE SVSNIFLSAE VAGRVHACHV GNGKILATFS TEGNIFSSLV VKTPPTFMGH
SFAIFGCIDQ HLYCLRCKTG PGGKSVELEL HWKVDVGAPI YATPTLLTVQ PNGLLVWCAA
TDGRVMLINF RNGEIQWSDK LPGQVFSSAC FIEDLRRVFV GCRDNFLYCL GI
